Literature DB >> 15502327

Crystallization and preliminary X-ray analysis of pyridoxal 4-dehydrogenase, the second enzyme in degradation pathway I of pyridoxine.

Nana Yokochi1, Yu Yoshikane, Toshiharu Yagi, Masayuki Yamasaki, Bunzo Mikami.   

Abstract

Pyridoxal 4-dehydrogenase (PLDH; EC 1.1.107) is the second enzyme in the bacterial degradation pathway I of vitamin B(6), which catalyzes the oxidation of pyridoxal to 4-pyridoxolactone using NAD(+). PLDH from Microbacterium luteolum, a dimeric protein with a subunit molecular weight of 38 kDa, was crystallized at 277 K in a drop solution comprising 15%(w/v) polyethylene glycol 4000, 0.15 M sodium acetate, 7.5 mM n-octyl-beta-D-glucoside and 0.075 M Tris-HCl pH 7.5 by the sitting-drop vapour-diffusion method. The crystals were monoclinic and belonged to space group C2, with unit-cell parameters a = 107.0, b = 56.7, c = 130.2 A, beta = 103.6 degrees . Diffraction data were collected from a single crystal to 2.0 A.

Entities:  

Mesh:

Substances:

Year:  2004        PMID: 15502327     DOI: 10.1107/S0907444904021754

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.

Authors:  Huy Nhat Chu; Jun Kobayashi; Yu Yoshikane; Bunzo Mikami; Toshiharu Yagi
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-05-29
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.